Molecular chaperones: a double-edged sword in neurodegenerative diseases

J Tittelmeier, E Nachman… - Frontiers in aging …, 2020 - frontiersin.org
Aberrant accumulation of misfolded proteins into amyloid deposits is a hallmark in many age-
related neurodegenerative diseases, including Alzheimer's disease (AD), Parkinson's …

The prion hypothesis: from biological anomaly to basic regulatory mechanism

MF Tuite, TR Serio - Nature reviews Molecular cell biology, 2010 - nature.com
Prions are unusual proteinaceous infectious agents that are typically associated with a class
of fatal degenerative diseases of the mammalian brain. However, the discovery of fungal …

Kinetic analysis reveals the diversity of microscopic mechanisms through which molecular chaperones suppress amyloid formation

P Arosio, TCT Michaels, S Linse, C Månsson… - Nature …, 2016 - nature.com
It is increasingly recognized that molecular chaperones play a key role in modulating the
formation of amyloid fibrils, a process associated with a wide range of human disorders …

Trehalose is a versatile and long-lived chaperone for desiccation tolerance

H Tapia, DE Koshland - Current Biology, 2014 - cell.com
Background Diverse organisms across taxa are desiccation tolerant, capable of surviving
extreme water loss. Remarkably, desiccation tolerant organisms can survive years without …

Prion switching in response to environmental stress

J Tyedmers, ML Madariaga, S Lindquist - PLoS biology, 2008 - journals.plos.org
Evolution depends on the manner in which genetic variation is translated into new
phenotypes. There has been much debate about whether organisms might have specific …

Mechanics of Hsp70 chaperones enables differential interaction with client proteins

R Schlecht, AH Erbse, B Bukau… - Nature structural & …, 2011 - nature.com
Hsp70 chaperones interact with a wide spectrum of substrates ranging from unfolded to
natively folded and aggregated proteins. Structural evidence suggests that bound substrates …

The HSP110/HSP70 disaggregation system generates spreading‐competent toxic α‐synuclein species

J Tittelmeier, CA Sandhof, HM Ries… - The EMBO …, 2020 - embopress.org
The accumulation and prion‐like propagation of α‐synuclein and other amyloidogenic
proteins are associated with devastating neurodegenerative diseases. Metazoan heat shock …

A heritable switch in carbon source utilization driven by an unusual yeast prion

JCS Brown, S Lindquist - Genes & development, 2009 - genesdev.cshlp.org
Several well-characterized fungal proteins act as prions, proteins capable of multiple
conformations, each with different activities, at least one of which is self-propagating …

Specificity of the J-protein Sis1 in the propagation of 3 yeast prions

T Higurashi, JK Hines, C Sahi… - Proceedings of the …, 2008 - National Acad Sciences
Yeast prions, such as [PSI+],[RNQ+], and [URE3], are heritable elements formed by proteins
capable of acquiring self-perpetuating conformations. Their propagation is dependent on …

In vivo monitoring of the prion replication cycle reveals a critical role for Sis1 in delivering substrates to Hsp104

KA Tipton, KJ Verges, JS Weissman - Molecular cell, 2008 - cell.com
Prions in Saccharomyces cerevisiae are inherited ordered aggregates reliant upon the
disaggregase Hsp104 for stable maintenance. The function of other factors in the natural …